Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Abz-KLKGAGQ-EDDnp + H2O
Abz-KLK + GAGQ-EDDnp
-
hydrolysis of FRET peptides
-
-
?
Edans-EGAVSVRSQEIK-Dabcyl + H2O
?
-
-
-
?
eukaryotic initiation factor 4G + H2O
?
-
Lbpro cleaves two homologues of the host cell protein. Lbpro possesses specific binding sites at the non-prime side from S1 down to S7
-
-
?
eukaryotic initiation factor eIF4G + H2O
?
eukaryotic initiation factor eIF4GI + H2O
?
eukaryotic initiation factor eIF4GII + H2O
?
eukaryotic translation initiation factor eIF4GI + H2O
?
foot-and-mouth disease leader protein + H2O
?
human cyclin A + H2O
?
-
-
-
-
?
mengovirus polypeptide + H2O
?
-
-
-
-
?
nisin + H2O
?
the final step in nisin maturation is the proteolytic cleavage of the first 23 amino-terminal residues by NisP
-
-
?
nisin-(leader peptide) + H2O
nisin + leader peptide
nuclear factor-kappaB + H2O
?
-
-
-
-
?
poliovirus replicase-related polypeptide + H2O
?
-
-
-
-
?
RNA helicase LGP2 + H2O
?
SFANLGRTTL + H2O
SFANLG + RTTL
poor substrate for both isoforms Lbpro and sLbpro
-
-
?
Val-Gln-Arg-Lys-Leu-Lys-4-methylcoumarin 7-amide + H2O
Val-Gln-Arg-Lys-Leu-Lys + 7-amino-4-methylcoumarin
-
the substrate corresponds to the six C-terminal amino acids of the leader protein
-
?
VQRKLGAAGQ + H2O
VQRKLG + AAGQ
isoform sLbpro cleaves this substrate better than isoform Lbpro
-
-
?
VQRKLGRAGQ + H2O
VQRKLG + RAGQ
isoform sLbpro cleaves this substrate better than isoform Lbpro
-
-
?
VQRKLKGAGQ + H2O
VQRKLK + GAGQ
isoform sLbpro cleaves this substrate better than isoform Lbpro
-
-
?
VQRKLKRAGQ + H2O
VQRKLK + RAGQ
isoform sLbpro cleaves this substrate better than isoform Lbpro
-
-
?
additional information
?
-
eukaryotic initiation factor eIF4G + H2O
?
-
-
-
-
?
eukaryotic initiation factor eIF4G + H2O
?
in intermolecular cleavage on polyprotein substrates, isoform Lbpro is unaffected by P1 or P1' substitutions and processes a substrate containing nine eIF4GI cleavage site residues whereas isoform sLbpro fails to cleave the eIF4GI containing substrate and cleaves appreciably more slowly on mutated substrates
-
-
?
eukaryotic initiation factor eIF4G + H2O
?
-
-
-
-
?
eukaryotic initiation factor eIF4GI + H2O
?
-
eukaryotic host cell protein substrate, cleavage prevents the synthesis of host cellular protein from capped cellular mRNAs, while the viral RNA is tsill translated initiating from an internal ribosome entry site
-
-
?
eukaryotic initiation factor eIF4GI + H2O
?
-
eukaryotic host cell protein substrate, recognition/cleavage site is ANLG*RTTL
-
-
?
eukaryotic initiation factor eIF4GI + H2O
?
-
eukaryotic host cell protein substrate, cleavage between residues G674 and R675, the enzyme binds to substrate residues 640-669 and interacts with C133 and residues 183-195, interaction analysis of enzyme with recombinant peptide fragments, reduced binding with mutated peptides K643A, K646A, and R650A overview
-
-
?
eukaryotic initiation factor eIF4GI + H2O
?
-
eukaryotic host cell protein substrate, recognition/cleavage site is ANLG*RTTL
-
-
?
eukaryotic initiation factor eIF4GI + H2O
?
-
eukaryotic host cell protein substrate, cleavage prevents the synthesis of host cellular protein from capped cellular mRNAs, while the viral RNA is tsill translated initiating from an internal ribosome entry site
-
-
?
eukaryotic initiation factor eIF4GI + H2O
?
-
eukaryotic host cell protein substrate, cleavage between residues G674 and R675, the enzyme binds to substrate residues 640-669 and interacts with C133 and residues 183-195, interaction analysis of enzyme with recombinant peptide fragments, reduced binding with mutated peptides K643A, K646A, and R650A overview
-
-
?
eukaryotic initiation factor eIF4GII + H2O
?
-
eukaryotic host cell protein substrate, cleavage prevents the synthesis of host cellular protein from capped cellular mRNAs, while the viral RNA is tsill translated initiating from an internal ribosome entry site
-
-
?
eukaryotic initiation factor eIF4GII + H2O
?
-
eukaryotic host cell protein substrate, recognition/cleavage site is LNVG*SRRS, but not ADFG*RQTP
-
-
?
eukaryotic initiation factor eIF4GII + H2O
?
-
eukaryotic host cell protein substrate
-
-
?
eukaryotic initiation factor eIF4GII + H2O
?
-
eukaryotic host cell protein substrate, recognition/cleavage site is LNVG*SRRS, but not ADFG*RQTP
-
-
?
eukaryotic initiation factor eIF4GII + H2O
?
-
eukaryotic host cell protein substrate, cleavage prevents the synthesis of host cellular protein from capped cellular mRNAs, while the viral RNA is tsill translated initiating from an internal ribosome entry site
-
-
?
eukaryotic initiation factor eIF4GII + H2O
?
-
eukaryotic host cell protein substrate
-
-
?
eukaryotic translation initiation factor eIF4GI + H2O
?
-
eukaryotic host cell protein substrate, cleavage causes the rapid inhibition of cellular cap-dependent protein synthesis
-
-
?
eukaryotic translation initiation factor eIF4GI + H2O
?
-
eukaryotic host cell protein substrate, cleavage causes the rapid inhibition of cellular cap-dependent protien synthesis
-
-
?
eukaryotic translation initiation factor eIF4GI + H2O
?
-
eukaryotic host cell protein substrate
-
-
?
eukaryotic translation initiation factor eIF4GI + H2O
?
-
eukaryotic host cell protein substrate, activity of 3Cpro and Lpro with wild-type and mutant substrate, overview, the highly specific 3Cpro cleavage site is located at the small 40-amino-acid region of the protein
-
-
?
eukaryotic translation initiation factor eIF4GI + H2O
?
-
eukaryotic host cell protein substrate, cleavage causes the rapid inhibition of cellular cap-dependent protein synthesis
-
-
?
eukaryotic translation initiation factor eIF4GI + H2O
?
-
eukaryotic host cell protein substrate
-
-
?
foot-and-mouth disease leader protein + H2O
?
-
-
-
-
?
foot-and-mouth disease leader protein + H2O
?
-
cis and trans cleavage activity at the L/P1 junction
-
-
?
foot-and-mouth disease leader protein + H2O
?
-
similar to other papain-like proteinases the enzyme possesses the catalytic cysteine and histidine residues, however the catalytic asparagine has been replaced by an aspartate. The interaction between the histidine and aspartate is exposed to solvent, as the tryptophan residues are missing. The cleavage site is between its own C-terminus and the N-terminus of VP4
-
-
?
nisin-(leader peptide) + H2O
nisin + leader peptide
-
-
-
?
nisin-(leader peptide) + H2O
nisin + leader peptide
after translocation into the extracellular space, the leader peptide is cleaved by the leader peptidase NisP, resulting in active nisin. NisP recognizes the cleavage site GASPR-/-IT located at the C-terminal end of the leader peptide
-
-
?
RNA helicase LGP2 + H2O
?
-
-
-
-
?
RNA helicase LGP2 + H2O
?
-
LGP2 cleavage by the Leader protease of aphthoviruses may represent an antagonistic mechanism for immune evasion
-
-
?
additional information
?
-
-
no hydrolysis of Phe-Arg-4-methylcoumarin 7-amide, Val-Lue-Lys-4-methylcoumarin 7-amide, classical papain substrates, or Ser-Phe-Ala-Asn-Leu-Gly-4-methylcoumarin 7-amide, corresponding to the N-terminal portion of the eIF4G cleavage site
-
-
?
additional information
?
-
-
the enzyme inhibits the immediate-early induction of beta interferon mRNA and blocks the host innate immune response by inhibition of IFN-induction of double-stranded RNA-dependent protein kinase R, 2',5'-oligoadenylate synthase, and Mx1 mRNAs in host porcine cells
-
-
?
additional information
?
-
-
elIF4GI cleavage site mapping
-
-
?
additional information
?
-
-
substrate recognition and cleavage site specificity, overview
-
-
?
additional information
?
-
-
the enzyme is synthesized as part of a large polyprotein LbproVP4VP, from which it releases itself by highly efficient self-processing between its C- and N-terminus of the subsequent protein VP4, recognition of the sequence QRKLK*GAGQ, specificity at the P2, Leu, and P3 positions, including S3 subsite preferring Lys or Asn, and comparison with other papain-like enzymes, no activity when Pro is at P2 position and with type I collagen, overview, residues P99, P100, L143, A149, and L178 determine the specificity of the S2 binding pocket
-
-
?
additional information
?
-
-
the leader protease, Lbpro, performs the initial cleavage by freeing itself from the growing polypeptide chain. Lbpro is not only one of the smallest papain-like cysteine peptidases but also one of the most specific. It has high prime side specificity at least down to the S' 5 site. It can still however cleave between both K-G and G-R pairs
-
-
?
additional information
?
-
-
the enzyme typically recognise the alternating positions of the side chains along the polypeptide sequence that are characteristic of an extended backbone conformation, and this serves to place the scissile bond in the correct orientation at the active site. Significant conformational adaptation by the enzyme is important for substrate recognition
-
-
?
additional information
?
-
-
the enzyme cleaves itself off the nascent viral polyprotein
-
-
?
additional information
?
-
-
the enzyme is synthesized as part of a large polyprotein LbproVP4VP, from which it releases itself by highly efficient self-processing between its C- and N-terminus of the subsequent protein VP4, recognition of the sequence QRKLK*GAGQ, specificity at the P2, Leu, and P3 positions, including S3 subsite preferring Lys or Asn, and comparison with other papain-like enzymes, no activity when Pro is at P2 position and with type I collagen, overview, residues P99, P100, L143, A149, and L178 determine the specificity of the S2 binding pocket
-
-
?
additional information
?
-
-
substrate recognition and cleavage site specificity, overview
-
-
?
additional information
?
-
-
the enzyme inhibits the immediate-early induction of beta interferon mRNA and blocks the host innate immune response by inhibition of IFN-induction of double-stranded RNA-dependent protein kinase R, 2',5'-oligoadenylate synthase, and Mx1 mRNAs in host porcine cells
-
-
?
additional information
?
-
the enzyme possesses an auto-cleavage site between residues Arg647 and Ser648
-
-
?
additional information
?
-
-
the enzyme possesses an auto-cleavage site between residues Arg647 and Ser648
-
-
?
translation initiation factor eIF4G + H2O
additional information
-
-
-
-
-
?
translation initiation factor eIF4G + H2O
additional information
-
-
-
-
-
?
translation initiation factor eIF4G + H2O
additional information
-
-
-
-
-
?
translation initiation factor eIF4G + H2O
additional information
-
-
-
characterization of cleavage products, primary cleavage of rabbit reticulocyte eIF-4-gamma occurs between Gly479-Arg480, complete proteolysis after 12 h
?
translation initiation factor eIF4G + H2O
additional information
-
-
very rapid reaction
-
-
?
translation initiation factor eIF4G + H2O
additional information
-
-
i.e. p220
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
eukaryotic initiation factor 4G + H2O
?
-
Lbpro cleaves two homologues of the host cell protein. Lbpro possesses specific binding sites at the non-prime side from S1 down to S7
-
-
?
eukaryotic initiation factor eIF4G + H2O
?
eukaryotic initiation factor eIF4GI + H2O
?
eukaryotic initiation factor eIF4GII + H2O
?
eukaryotic translation initiation factor eIF4GI + H2O
?
foot-and-mouth disease leader protein + H2O
?
nisin + H2O
?
the final step in nisin maturation is the proteolytic cleavage of the first 23 amino-terminal residues by NisP
-
-
?
nisin-(leader peptide) + H2O
nisin + leader peptide
after translocation into the extracellular space, the leader peptide is cleaved by the leader peptidase NisP, resulting in active nisin. NisP recognizes the cleavage site GASPR-/-IT located at the C-terminal end of the leader peptide
-
-
?
nuclear factor-kappaB + H2O
?
-
-
-
-
?
RNA helicase LGP2 + H2O
?
-
LGP2 cleavage by the Leader protease of aphthoviruses may represent an antagonistic mechanism for immune evasion
-
-
?
additional information
?
-
eukaryotic initiation factor eIF4G + H2O
?
-
-
-
-
?
eukaryotic initiation factor eIF4G + H2O
?
in intermolecular cleavage on polyprotein substrates, isoform Lbpro is unaffected by P1 or P1' substitutions and processes a substrate containing nine eIF4GI cleavage site residues whereas isoform sLbpro fails to cleave the eIF4GI containing substrate and cleaves appreciably more slowly on mutated substrates
-
-
?
eukaryotic initiation factor eIF4G + H2O
?
-
-
-
-
?
eukaryotic initiation factor eIF4GI + H2O
?
-
eukaryotic host cell protein substrate, cleavage prevents the synthesis of host cellular protein from capped cellular mRNAs, while the viral RNA is tsill translated initiating from an internal ribosome entry site
-
-
?
eukaryotic initiation factor eIF4GI + H2O
?
-
eukaryotic host cell protein substrate, recognition/cleavage site is ANLG*RTTL
-
-
?
eukaryotic initiation factor eIF4GI + H2O
?
-
eukaryotic host cell protein substrate, recognition/cleavage site is ANLG*RTTL
-
-
?
eukaryotic initiation factor eIF4GI + H2O
?
-
eukaryotic host cell protein substrate, cleavage prevents the synthesis of host cellular protein from capped cellular mRNAs, while the viral RNA is tsill translated initiating from an internal ribosome entry site
-
-
?
eukaryotic initiation factor eIF4GII + H2O
?
-
eukaryotic host cell protein substrate, cleavage prevents the synthesis of host cellular protein from capped cellular mRNAs, while the viral RNA is tsill translated initiating from an internal ribosome entry site
-
-
?
eukaryotic initiation factor eIF4GII + H2O
?
-
eukaryotic host cell protein substrate, recognition/cleavage site is LNVG*SRRS, but not ADFG*RQTP
-
-
?
eukaryotic initiation factor eIF4GII + H2O
?
-
eukaryotic host cell protein substrate, recognition/cleavage site is LNVG*SRRS, but not ADFG*RQTP
-
-
?
eukaryotic initiation factor eIF4GII + H2O
?
-
eukaryotic host cell protein substrate, cleavage prevents the synthesis of host cellular protein from capped cellular mRNAs, while the viral RNA is tsill translated initiating from an internal ribosome entry site
-
-
?
eukaryotic translation initiation factor eIF4GI + H2O
?
-
eukaryotic host cell protein substrate, cleavage causes the rapid inhibition of cellular cap-dependent protein synthesis
-
-
?
eukaryotic translation initiation factor eIF4GI + H2O
?
-
eukaryotic host cell protein substrate, cleavage causes the rapid inhibition of cellular cap-dependent protien synthesis
-
-
?
eukaryotic translation initiation factor eIF4GI + H2O
?
-
eukaryotic host cell protein substrate, cleavage causes the rapid inhibition of cellular cap-dependent protein synthesis
-
-
?
foot-and-mouth disease leader protein + H2O
?
-
-
-
-
?
foot-and-mouth disease leader protein + H2O
?
-
cis and trans cleavage activity at the L/P1 junction
-
-
?
foot-and-mouth disease leader protein + H2O
?
-
similar to other papain-like proteinases the enzyme possesses the catalytic cysteine and histidine residues, however the catalytic asparagine has been replaced by an aspartate. The interaction between the histidine and aspartate is exposed to solvent, as the tryptophan residues are missing. The cleavage site is between its own C-terminus and the N-terminus of VP4
-
-
?
additional information
?
-
-
the enzyme inhibits the immediate-early induction of beta interferon mRNA and blocks the host innate immune response by inhibition of IFN-induction of double-stranded RNA-dependent protein kinase R, 2',5'-oligoadenylate synthase, and Mx1 mRNAs in host porcine cells
-
-
?
additional information
?
-
-
the leader protease, Lbpro, performs the initial cleavage by freeing itself from the growing polypeptide chain. Lbpro is not only one of the smallest papain-like cysteine peptidases but also one of the most specific. It has high prime side specificity at least down to the S' 5 site. It can still however cleave between both K-G and G-R pairs
-
-
?
additional information
?
-
-
the enzyme cleaves itself off the nascent viral polyprotein
-
-
?
additional information
?
-
-
the enzyme inhibits the immediate-early induction of beta interferon mRNA and blocks the host innate immune response by inhibition of IFN-induction of double-stranded RNA-dependent protein kinase R, 2',5'-oligoadenylate synthase, and Mx1 mRNAs in host porcine cells
-
-
?
additional information
?
-
the enzyme possesses an auto-cleavage site between residues Arg647 and Ser648
-
-
?
additional information
?
-
-
the enzyme possesses an auto-cleavage site between residues Arg647 and Ser648
-
-
?
translation initiation factor eIF4G + H2O
additional information
-
-
-
-
-
?
translation initiation factor eIF4G + H2O
additional information
-
-
-
-
-
?
translation initiation factor eIF4G + H2O
additional information
-
-
-
-
-
?
translation initiation factor eIF4G + H2O
additional information
-
-
-
characterization of cleavage products, primary cleavage of rabbit reticulocyte eIF-4-gamma occurs between Gly479-Arg480, complete proteolysis after 12 h
?
translation initiation factor eIF4G + H2O
additional information
-
-
very rapid reaction
-
-
?
translation initiation factor eIF4G + H2O
additional information
-
-
i.e. p220
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Kirchweger, R.; Ziegler, E.; Lamphear, B.J.; Waters, D.; Liebig, H.D.; Sommergruber, W.; Sobrino, F.; Hohenadl, C.; Blaas, D.; Rhoads, R.E.; Skern, T.
Foot-and-mouth disease virus leader proteinase: purification of the Lb form and determination of its cleavage site on eIF-4gamma
J. Virol.
68
5677-5684
1994
Foot-and-mouth disease virus
brenda
Piccone, M.E.; Zellner, M.; Kumosinski, T.F.; Mason, P.W.; Grubman, M.J.
Identification of the active-site residues of the L proteinase of foot-and-mouth disease virus
J. Virol.
69
4950-4956
1995
Foot-and-mouth disease virus
brenda
Guarne, A.; Hampoelz, B.; Glaser, W.; Carpena, X.; Torma, J.; Fita, I.; Skern, T.
Structural and biochemical features distinguish the foot-and-mouth disease virus leader proteinase from other papain-like enzymes
J. Mol. Biol.
302
1227-1240
2000
Foot-and-mouth disease virus
brenda
Glaser, W.; Skern, T.
Extremely efficient cleavage of eIF4G by picornaviral proteinases L and 2A in vitro
FEBS Lett.
480
151-155
2000
Foot-and-mouth disease virus
brenda
Guarne, A.; Tormo, J.; Kirchweger, R.; Pfistermueller, D.; Fita, I.; Skern, T.
Structure of the foot-and-mouth disease virus leader protease: a papain-like fold adapted for self-processing and eIF4G recognition
EMBO J.
17
7469-7479
1998
Foot-and-mouth disease virus
brenda
Piccone, M.E.; Sira, S.; Zellner, M.; Grubman, M.J.
Expression in Escherichia coli and purification of biologically active L proteinase of foot-and-mouth disease virus
Virus Res.
35
263-275
1995
Foot-and-mouth disease virus
brenda
Skern, T.; Fita, I.; Guarne, A.
A structural model of picornavirus leader proteinases based on papain and bleomycin hydrolase
J. Gen. Virol.
79
301-307
1998
Foot-and-mouth disease virus
brenda
Ziegler, E.; Borman, A.M.; Kirchweger, R.; Skern, T.; Kean, K.M.
Foot-and-mouth disease virus Lb proteinase can stimulate rhinovirus and enterovirus IRES-driven translation and cleave several proteins of cellular and viral origin
J. Virol.
69
3465-3474
1995
Foot-and-mouth disease virus
brenda
Kuehnel, E.; Cencic, R.; Foeger, N.; Skern, T.
Foot-and-mouth disease virus leader proteinase: specificity at the P2 and P3 positions and comparison with other papain-like enzymes
Biochemistry
43
11482-11490
2004
Foot-and-mouth disease virus, Foot-and-mouth disease virus FMDV
brenda
Foeger, N.; Kuehnel, E.; Cencic, R.; Skern, T.
The binding of foot-and-mouth disease virus leader proteinase to eIF4GI involves conserved ionic interactions
FEBS J.
272
2602-2611
2005
Foot-and-mouth disease virus, Foot-and-mouth disease virus FMDV
brenda
Strong, R.; Belsham, G.J.
Sequential modification of translation initiation factor eIF4GI by two different foot-and-mouth disease virus proteases within infected baby hamster kidney cells: Identification of the 3Cpro cleavage site
J. Gen. Virol.
85
3817
2004
Foot-and-mouth disease virus
-
brenda
de Los Santos, T.; de Avila Botton, S.; Weiblen, R.; Grubman, M.J.
The leader proteinase of foot-and-mouth disease virus inhibits the induction of beta interferon mRNA and blocks the host innate immune response
J. Virol.
80
1906-1914
2006
Foot-and-mouth disease virus, Foot-and-mouth disease virus FMDV
brenda
Cencic, R.; Mayer, C.; Juliano, M.A.; Juliano, L.; Konrat, R.; Kontaxis, G.; Skern, T.
Investigating the substrate specificity and oligomerisation of the leader protease of foot and mouth disease virus using NMR
J. Mol. Biol.
373
1071-1087
2007
Foot-and-mouth disease virus
brenda
de Los Santos, T.; Diaz-San Segundo, F.; Grubman, M.J.
Degradation of nuclear factor kappa B during foot-and-mouth disease virus infection
J. Virol.
81
12803-12815
2007
Foot-and-mouth disease virus
brenda
Mayer, C.; Neubauer, D.; Nchinda, A.T.; Cencic, R.; Trompf, K.; Skern, T.
Residue L143 of the foot-and-mouth disease virus leader proteinase is a determinant of cleavage specificity
J. Virol.
82
4656-4659
2008
Foot-and-mouth disease virus (P03305)
brenda
Zunszain, P.A.; Knox, S.R.; Sweeney, T.R.; Yang, J.; Roque-Rosell, N.; Belsham, G.J.; Leatherbarrow, R.J.; Curry, S.
Insights into cleavage specificity from the crystal structure of foot-and-mouth disease virus 3C protease complexed with a peptide substrate
J. Mol. Biol.
395
375-389
2010
Foot-and-mouth disease virus
brenda
Wang, D.; Fang, L.; Luo, R.; Ye, R.; Fang, Y.; Xie, L.; Chen, H.; Xiao, S.
Foot-and-mouth disease virus leader proteinase inhibits dsRNA-induced type I interferon transcription by decreasing interferon regulatory factor 3/7 in protein levels
Biochem. Biophys. Res. Commun.
399
72-78
2010
Foot-and-mouth disease virus
brenda
Nogueira Santos, J.A.; Assis, D.M.; Gouvea, I.E.; Judice, W.A.; Izidoro, M.A.; Juliano, M.A.; Skern, T.; Juliano, L.
Foot and mouth disease leader protease (Lb(pro)): Investigation of prime side specificity allows the synthesis of a potent inhibitor
Biochimie
94
711-718
2011
Foot-and-mouth disease virus
brenda
Piccone, M.E.; Diaz-San Segundo, F.; Kramer, E.; Rodriguez, L.L.; de los Santos, T.
Introduction of tag epitopes in the inter-AUG region of foot and mouth disease virus: effect on the L protein
Virus Res.
155
91-97
2011
Foot-and-mouth disease virus
brenda
Xu, Y.; Li, X.; Li, R.; Li, S.; Ni, H.; Wang, H.; Xu, H.; Zhou, W.; Saris, P.E.; Yang, W.; Qiao, M.; Rao, Z.
Structure of the nisin leader peptidase NisP revealing a C-terminal autocleavage activity
Acta Crystallogr. Sect. D
70
1499-1505
2014
Lactococcus lactis (D9IXC0), Lactococcus lactis
brenda
Dhiman, H.; Dhanjal, J.K.; Sharma, S.; Chacko, S.; Grover, S.; Grover, A.
Resisting resistant Mycobacterium tuberculosis naturally: mechanistic insights into the inhibition of the parasites sole signal peptidase Leader peptidase B
Biochem. Biophys. Res. Commun.
433
552-557
2013
Mycobacterium tuberculosis (P9WKA1), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WKA1)
brenda
Steinberger, J.; Skern, T.
The leader proteinase of foot-and-mouth disease virus: structure-function relationships in a proteolytic virulence factor
Biol. Chem.
395
1179-1185
2014
Foot-and-mouth disease virus
brenda
Steinberger, J.; Kontaxis, G.; Rancan, C.; Skern, T.
Comparison of self-processing of foot-and-mouth disease virus leader proteinase and porcine reproductive and respiratory syndrome virus leader proteinase nsp1alpha
Virology
443
271-277
2013
Foot-and-mouth disease virus, porcine reproductive and respiratory syndrome virus
brenda
Steinberger, J.; Grishkovskaya, I.; Cencic, R.; Juliano, L.; Juliano, M.A.; Skern, T.
Foot-and-mouth disease virus leader proteinase: structural insights into the mechanism of intermolecular cleavage
Virology
468-470
397-408
2014
Foot-and-mouth disease virus (P03305)
brenda
Shan, H.; Pasin, F.; Valli, A.; Castillo, C.; Rajulu, C.; Carbonell, A.; Simon-Mateo, C.; Garcia, J.A.; Rodamilans, B.
The Potyviridae P1a leader protease contributes to host range specificity
Virology
476
264-270
2015
cucumber vein yellowing virus (Q1G2C1), cucumber vein yellowing virus
brenda
Lagedroste, M.; Smits, S.H.J.; Schmitt, L.
Substrate specificity of the secreted nisin leader peptidase NisP
Biochemistry
56
4005-4014
2017
Lactococcus lactis subsp. lactis (Q07596)
brenda
Rodriguez Pulido, M.; Sanchez-Aparicio, M.T.; Martinez-Salas, E.; Garcia-Sastre, A.; Sobrino, F.; Saiz, M.
Innate immune sensor LGP2 is cleaved by the Leader protease of foot-and-mouth disease virus
PLoS Pathog.
14
e1007135
2018
Foot-and-mouth disease virus
brenda
Atallah, O.; Kang, S.; El-Mohtar, C.; Shilts, T.; Bergua, M.; Folimonova, S.
A 5-proximal region of the Citrus tristeza virus genome encoding two leader proteases is involved in virus superinfection exclusion
Virology
489
108-115
2016
Citrus tristeza virus
brenda